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Online Journal of Bioinformatics©
Volume 22 (3): 165-174, 2021.
In-silico polymorphism and structure of human retinal-aldehyde-binding protein 1.
Muhammad Ilyas and Khalid Masood
National Center of Excellence in Molecular Biology, University of the Punjab, Lahore, Bioinformatics Laboratory, National Center of Excellence in Molecular Biology, University of the Punjab Lahore India
Ilyas M, Masood K., In-silico polymorphism and structure of human retinal-aldehyde-binding protein 1,, Onl J Bioinform., 22 (3): 175-188, 2021. Cellular retinaldehyde binding protein (CRALBP), a 36-kD water-soluble protein occurs in retina and pineal gland with 11-cis- retinaldehyde or 11-cis-retinal ligands. Human retinal-aldehyde-binding protein 1 (RLBP1) gene was searched for single nucleotide polymorphisms (SNP) revealing 116 of 3 non-synonymous (nsSNP) and 1 in synonymous regions. Non-coding areas comprised 7 SNPs in UTR and 98 in introns. The 3 nsSNPs transcription factor binding sites included G/A SNP, arginine to glutamine substitution, C/T SNP arginine to tryptophan and C/G/A SNP histidine to glutamine. The model revealed SNP position 151, 234 and 269 mutated for changes in protein structure. Model hydrogen bonding, ion pairs and accessibility are described. We report In silico association of RLBP1 SNPs with night vision blindness, Bothnia retinal and Newfoundland rod-cone dystrophies and Fundus Albipunctatus. Mutations in the domain could decrease the interactions between the residues causing unstability.
Key words: RLBP1, nsSNPs, Homology modeling, 11-cis- retinaldehyde.